Young-Nam Park

Replacements of Amino Acid Residues at Subsites and Their Effects on the Catalytic Properties of Rhizomucor pusillus Pepsin, an Aspartic Proteinase from Rhizomucor pusillus (2001)

Aikawa, Jun-ichi, Park, Young-Nam, Sugiyama, Masakazu, Nishiyama, Makoto, Horinouchi, Sueharu, Beppu, Teruhiko

Site-directed mutagenesis was carried out to investigate the functional roles of amino acid residues of Rhizomucor pusillus pepsin (RMPP) in substrate-binding and catalysis. Mutations of two amino...

Site-Directed Mutagenesis of Conserved Trp39 in Rhizomucor pusillus Pepsin: Possible Role of Trp39 in Maintaining Tyr75 in the Correct Orientation for Maximizing Catalytic Activity (1997)

Park, Young-Nam, Aikawa, Jun-ichi, Nishiyama, Makoto, Horinouchi, Sueharu, Beppu, Teruhiko

Replacement of Trp39 of Rhizomucor pusillus pepsin (RMPP) by Asn or Cys resulted in a marked decrease in the milk-clotting and proteolytic activities. Kinetic analysis with chromogenic synthetic...

Involvement of a residue at position 75 in the catalytic mechanism of a fungal aspartic proteinase, Rhizomucor pusilus pepsin. Replacement of tyrosine 75 on the flap by asparagine enhances catalytic efficiency (1996)

Park, Young-Nam, Aikawa, Jun-ichi, Nishiyama, Makoto, Horinouchi, Sueharu, Beppu, Teruhiko

Residue 75 on the flap, a beta hairpin loop that partially covers the active site cleft, is tyrosine in most members of the aspartic proteinase family. Site-directed mutagenesis was carried out to...

A single amino acid change in the acetylcholinesterase-like domain of thyroglobulin causes congenital goiter with hypothyroidism in the cog/cog mouse: A model of human endoplasmic reticulum storage diseases

Kim, Paul S., Hossain, Shaikh Abu, Park, Young-Nam, Lee, Ike, Yoo, Sung-Eun, Arvan, Peter

Newly synthesized thyroglobulin (Tg), the major secretory glycoprotein of the thyroid gland, folds and homodimerizes in the endoplasmic reticulum (ER) before its export to the site of iodination,...

Mixed-Disulfide Folding Intermediates between Thyroglobulin and Endoplasmic Reticulum Resident Oxidoreductases ERp57 and Protein Disulfide Isomerase

Di Jeso, Bruno, Park, Young-nam, Ulianich, Luca, Treglia, A. Sonia, Urbanas, Malene L., High, Stephen, ...

We present the first identification of transient folding intermediates of endogenous thyroglobulin (Tg; a large homodimeric secretory glycoprotein of thyrocytes), which include mixed disulfides with...

A single amino acid change in the acetylcholinesterase-like domain of thyroglobulin causes congenital goiter with hypothyroidism in the cog/cog mouse: A model of human endoplasmic reticulum storage diseases

Kim, Paul S., Hossain, Shaikh Abu, Park, Young-Nam, Lee, Ike, Yoo, Sung-Eun, Arvan, Peter

Newly synthesized thyroglobulin (Tg), the major secretory glycoprotein of the thyroid gland, folds and homodimerizes in the endoplasmic reticulum (ER) before its export to the site of iodination,...

Mixed-Disulfide Folding Intermediates between Thyroglobulin and Endoplasmic Reticulum Resident Oxidoreductases ERp57 and Protein Disulfide Isomerase

Di Jeso, Bruno, Park, Young-nam, Ulianich, Luca, Treglia, A. Sonia, Urbanas, Malene L., High, Stephen, ...

We present the first identification of transient folding intermediates of endogenous thyroglobulin (Tg; a large homodimeric secretory glycoprotein of thyrocytes), which include mixed disulfides with...

Protein disulfide isomerase–like proteins play opposing roles during retrotranslocation

Forster, Michele L., Sivick, Kelsey, Park, Young-nam, Arvan, Peter, Lencer, Wayne I., Tsai, Billy

Misfolded proteins in the endoplasmic reticulum (ER) are retained in the organelle or retrotranslocated to the cytosol for proteasomal degradation. ER chaperones that guide these opposing processes...